Laminin subunit alpha-4
Domain
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain G is globular.
Function
Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Involvement in disease
Cardiomyopathy, dilated, 1JJ
CMD1JJ
A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
None
The disease is caused by variants affecting the gene represented in this entry.
Tissue Specificity
Detected in placenta (at protein level) (PubMed:32337544). Detected in fibroblasts and urine (at protein level) (PubMed:25326458, PubMed:36213313, PubMed:37453717). In adult, strong expression in heart, lung, ovary small and large intestines, placenta, liver; weak or no expression in skeletal muscle, kidney, pancreas, testis, prostate, brain. High expression in fetal lung and kidney. Expression in fetal and newborn tissues is observed in certain mesenchymal cells in tissues such as smooth muscle and dermis.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
- Basement membrane
- Secreted
- Major basement membrane component.
Alternative names
Laminin subunit alpha-4, Laminin-14 subunit alpha, Laminin-8 subunit alpha, Laminin-9 subunit alpha, LAMA4